4.7 Article

Isolation and identification of novel antibacterial peptides produced by Lactobacillus fermentum SHY10 in Chinese pickles

期刊

FOOD CHEMISTRY
卷 348, 期 -, 页码 -

出版社

ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2021.129097

关键词

Antibacterial peptides; Lactobacillus fermentum; Chinese pickles; Molecular docking

资金

  1. Key Research and Development Projects in Tibet: Preservation of Characteristic Biological Germplasm Resources and Utilization of Gene Technology in Tibet [XZ202001ZY00N]
  2. Chongqing Innovative Team of Modern Mountain Features Efficient Agricultural Technology System 2020 (5)
  3. Fundamental Research Funds for the Central Universities [SWU019026]

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This study aimed to isolate and identify antibacterial peptides produced by lactic acid bacteria in Chinese pickles. A total of 14 LAB strains with antibacterial activity were identified, among which L. fermentum SHY10 exhibited the most effective antibacterial activity. LC-MS/MS identified three novel ABPs, with the NQGPLGNAHR peptide showing significant antibacterial activity. Molecular docking analysis revealed the interaction of this peptide with DNA gyrase and dihydrofolate reductase.
The aim of this study was to isolate and identify antibacterial peptides (ABPs) produced by lactic acid bacteria (LAB) in Chinese pickles. The cell-free supernatant collected from the culture of LAB with antibacterial activity against Staphylococcus aureus was used to purify ABPs. A total of 14 strains of LAB were found to have antibacterial activity. Among them, Lactobacillus fermentum (L. fermentum) SHY10 exhibited the most effective antibacterial activity. The antibacterial activity of cell-free supernatant reached the highest level after 20 h of L. fermentum SHY10 culture. Three novel ABPs were identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS). In particular, the NQGPLGNAHR peptide showed antibacterial activity with an IC50 value of 0.957 mg/mL. In addition, molecular docking analysis revealed that this peptide interacted with DNA gyrase and dihydrofolate reductase by salt bridge formation, hydrogen bond interactions, and metal contact.

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